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Fragilysin (EC 3.4.24.74,Bacteroides fragilis (entero)toxin) is anenzyme.^[1]^[2]^[3]^[4]^[5] This enzymecatalyses the followingchemical reaction

Broadproteolytic specificity, bondshydrolysed including -Gly-Leu-, -Met-Leu-, -Phe-Leu-, -Cys-Leu-, Leu-Gly

It is thought to be a cause ofdiarrhoea in animals and humans.

References

^Moncrief JS, Obiso R, Barroso LA, Kling JJ, Wright RL, Van Tassell RL, Lyerly DM, Wilkins TD (January 1995)."The enterotoxin of Bacteroides fragilis is a metalloprotease".Infection and Immunity.63 (1):175–81.doi:10.1128/iai.63.1.175-181.1995.PMC 172975.PMID 7806355.
^Obiso RJ, Lyerly DM, Van Tassell RL, Wilkins TD (October 1995)."Proteolytic activity of the Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo".Infection and Immunity.63 (10):3820–6.doi:10.1128/iai.63.10.3820-3826.1995.PMC 173537.PMID 7558286.
^Donelli G, Fabbri A, Fiorentini C (January 1996)."Bacteroides fragilis enterotoxin induces cytoskeletal changes and surface blebbing in HT-29 cells".Infection and Immunity.64 (1):113–9.doi:10.1128/iai.64.1.113-119.1996.PMC 173735.PMID 8557328.
^Koshy SS, Montrose MH, Sears CL (December 1996)."Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroides fragilis".Infection and Immunity.64 (12):5022–8.doi:10.1128/iai.64.12.5022-5028.1996.PMC 174483.PMID 8945541.
^Kling JJ, Wright RL, Moncrief JS, Wilkins TD (January 1997)."Cloning and characterization of the gene for the metalloprotease enterotoxin of Bacteroides fragilis".FEMS Microbiology Letters.146 (2):279–84.doi:10.1016/s0378-1097(96)00488-0.PMID 9011050.

Fragilysin at the U.S. National Library of MedicineMedical Subject Headings (MeSH)

v t e Proteases:metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)